Site-Specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis. Issue 4 (19th February 2015)
- Record Type:
- Journal Article
- Title:
- Site-Specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis. Issue 4 (19th February 2015)
- Main Title:
- Site-Specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis
- Authors:
- Hu, Jiliang
Huang, Xiahe
Chen, Lichao
Sun, Xuwu
Lu, Congming
Zhang, Lixin
Wang, Yingchun
Zuo, Jianru - Abstract:
- Abstract : Proteome-wide identification of S-nitrosylated proteins in Arabidopsis by nitrosoproteomic analysis reveals the involvement of S-nitrosylation in diverse signaling pathways. Abstract: Nitric oxide (NO ) regulates multiple developmental events and stress responses in plants. A major biologically active species of NO is S -nitrosoglutathione (GSNO ), which is irreversibly degraded by GSNO reductase (GSNOR). The major physiological effect of NO is protein S -nitrosylation, a redox-based posttranslational modification mechanism by covalently linking an NO molecule to a cysteine thiol. However, little is known about the mechanisms of S -nitrosylation-regulated signaling, partly due to limited S -nitrosylated proteins being identified. In this study, we identified 1, 195 endogenously S -nitrosylated peptides in 926 proteins from the Arabidopsis ( Arabidopsis thaliana ) by a site-specific nitrosoproteomic approach, which, to date, is the largest data set of S -nitrosylated proteins among all organisms. Consensus sequence analysis of these peptides identified several motifs that contain acidic, but not basic, amino acid residues flanking the S -nitrosylated cysteine residues. These S -nitrosylated proteins are involved in a wide range of biological processes and are significantly enriched in chlorophyll metabolism, photosynthesis, carbohydrate metabolism, and stress responses. Consistently, the gsnor1-3 mutant shows the decreased chlorophyll content and alteredAbstract : Proteome-wide identification of S-nitrosylated proteins in Arabidopsis by nitrosoproteomic analysis reveals the involvement of S-nitrosylation in diverse signaling pathways. Abstract: Nitric oxide (NO ) regulates multiple developmental events and stress responses in plants. A major biologically active species of NO is S -nitrosoglutathione (GSNO ), which is irreversibly degraded by GSNO reductase (GSNOR). The major physiological effect of NO is protein S -nitrosylation, a redox-based posttranslational modification mechanism by covalently linking an NO molecule to a cysteine thiol. However, little is known about the mechanisms of S -nitrosylation-regulated signaling, partly due to limited S -nitrosylated proteins being identified. In this study, we identified 1, 195 endogenously S -nitrosylated peptides in 926 proteins from the Arabidopsis ( Arabidopsis thaliana ) by a site-specific nitrosoproteomic approach, which, to date, is the largest data set of S -nitrosylated proteins among all organisms. Consensus sequence analysis of these peptides identified several motifs that contain acidic, but not basic, amino acid residues flanking the S -nitrosylated cysteine residues. These S -nitrosylated proteins are involved in a wide range of biological processes and are significantly enriched in chlorophyll metabolism, photosynthesis, carbohydrate metabolism, and stress responses. Consistently, the gsnor1-3 mutant shows the decreased chlorophyll content and altered photosynthetic properties, suggesting that S -nitrosylation is an important regulatory mechanism in these processes. These results have provided valuable resources and new clues to the studies on S -nitrosylation-regulated signaling in plants. … (more)
- Is Part Of:
- Plant physiology. Volume 167:Issue 4(2015)
- Journal:
- Plant physiology
- Issue:
- Volume 167:Issue 4(2015)
- Issue Display:
- Volume 167, Issue 4 (2015)
- Year:
- 2015
- Volume:
- 167
- Issue:
- 4
- Issue Sort Value:
- 2015-0167-0004-0000
- Page Start:
- 1731
- Page End:
- 1746
- Publication Date:
- 2015-02-19
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.15.00026 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 22167.xml